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  • Title: Residual native structure in a thermally denatured beta-hairpin.
    Author: Smith AW, Chung HS, Ganim Z, Tokmakoff A.
    Journal: J Phys Chem B; 2005 Sep 15; 109(36):17025-7. PubMed ID: 16853169.
    Abstract:
    We investigate the thermal denaturation of trpzip2 between 15 and 82 degrees C using two-dimensional infrared (2D IR) vibrational spectroscopy, dispersed vibrational echo (DVE) spectroscopy, and Fourier transform infrared (FTIR) spectroscopy. The FTIR and DVE spectra of trpzip2 show in the amide I region of the spectrum two resonances, which arise primarily from the interstrand coupling between local amide I oscillators along the peptide backbone. The coupling is seen directly in the 2D IR spectra as the formation of cross-peak ridges. Although small shifts of these frequencies occur on heating the sample, the existence of cross-peak ridges at all temperatures indicates that stable hydrogen bond interactions persist between the two beta-strands. These observations indicate a significant amount of native structure in the thermally denatured state of trpzip2.
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